› 2x0r

X-ray diffraction
2.92Å resolution

R207S, R292S Mutant of Malate Dehydrogenase from the Halophilic Archeon Haloarcula marismortui (HoloForm)

Released:
DOI: 10.2210/pdb2x0r/pdb
PDB entry 2x0r coloured by chain, front view.
PDB entry 2x0r coloured by chain, side view.
PDB entry 2x0r coloured by chain, top view.
Source organism: Haloarcula marismortui
Primary publication:
The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies.
Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FM
J Mol Biol 326 859-73 (2003)
PMID: 12581646

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 32.7 KDa
Source organism: Haloarcula marismortui
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07841 (Residues: 1-304; Coverage: 100%)
Gene names: mdh, rrnAC2706
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand CL 4 x CL
Ligand NA 5 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NONIUS
Spacegroup: C2221
Unit cell:
a: 115.36Å b: 125.91Å c: 125.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.286
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Halophiles and their enzymes: negativity put to good use.
DasSarma et al. (2015)
3 more